ANXA8_HUMAN
ID ANXA8_HUMAN Reviewed; 327 AA.
AC P13928; A6NDE6; A6NLM1; B4DKI1; B4DTC9; Q5T2P8; Q5VTM4; Q6GMY3; Q9BT34;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Annexin A8 {ECO:0000312|HGNC:HGNC:546};
DE AltName: Full=Annexin VIII {ECO:0000303|PubMed:1313714};
DE AltName: Full=Annexin-8 {ECO:0000303|PubMed:2530088};
DE AltName: Full=Vascular anticoagulant-beta {ECO:0000303|PubMed:2530088};
DE Short=VAC-beta {ECO:0000303|PubMed:2530088};
GN Name=ANXA8 {ECO:0000312|HGNC:HGNC:546}; Synonyms=ANX8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-6 AND ALA-177.
RC TISSUE=Placenta;
RX PubMed=2530088; DOI=10.1111/j.1432-1033.1989.tb15082.x;
RA Hauptmann R., Maurer-Fogy I., Krystek E., Bodo G., Andree H.,
RA Reutelingsperger C.P.M.;
RT "Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding
RT protein that inhibits coagulation and phospholipase A2 activity. Its
RT molecular cloning, expression and comparison with VAC-alpha.";
RL Eur. J. Biochem. 185:63-71(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1313714;
RA Chang K.S., Wang G., Freireich E.J., Daly M., Naylor S.L., Trujillo J.M.,
RA Stass S.A.;
RT "Specific expression of the annexin VIII gene in acute promyelocytic
RT leukemia.";
RL Blood 79:1802-1810(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Cervix, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-177.
RC TISSUE=Lung, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), AND CALCIUM-BINDING SITES.
RX PubMed=15644210; DOI=10.1016/j.jmb.2004.11.015;
RA Rety S., Sopkova-de Oliveira Santos J., Dreyfuss L., Blondeau K.,
RA Hofbauerova K., Raguenes-Nicol C., Kerboeuf D., Renouard M.,
RA Russo-Marie F., Lewit-Bentley A.;
RT "The crystal structure of annexin A8 is similar to that of annexin A3.";
RL J. Mol. Biol. 345:1131-1139(2005).
CC -!- FUNCTION: This protein is an anticoagulant protein that acts as an
CC indirect inhibitor of the thromboplastin-specific complex, which is
CC involved in the blood coagulation cascade.
CC -!- INTERACTION:
CC P13928; P54253: ATXN1; NbExp=6; IntAct=EBI-2556915, EBI-930964;
CC P13928; P46379-2: BAG6; NbExp=3; IntAct=EBI-2556915, EBI-10988864;
CC P13928; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-2556915, EBI-21553822;
CC P13928; O14645: DNALI1; NbExp=3; IntAct=EBI-2556915, EBI-395638;
CC P13928; Q01658: DR1; NbExp=3; IntAct=EBI-2556915, EBI-750300;
CC P13928; Q00403: GTF2B; NbExp=3; IntAct=EBI-2556915, EBI-389564;
CC P13928; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-2556915, EBI-1054873;
CC P13928; P04792: HSPB1; NbExp=3; IntAct=EBI-2556915, EBI-352682;
CC P13928; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2556915, EBI-10975473;
CC P13928; O14901: KLF11; NbExp=3; IntAct=EBI-2556915, EBI-948266;
CC P13928; P07196: NEFL; NbExp=3; IntAct=EBI-2556915, EBI-475646;
CC P13928; O43933: PEX1; NbExp=3; IntAct=EBI-2556915, EBI-988601;
CC P13928; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2556915, EBI-25882629;
CC P13928; P60891: PRPS1; NbExp=3; IntAct=EBI-2556915, EBI-749195;
CC P13928; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2556915, EBI-396669;
CC P13928; P00441: SOD1; NbExp=3; IntAct=EBI-2556915, EBI-990792;
CC P13928; Q13148: TARDBP; NbExp=6; IntAct=EBI-2556915, EBI-372899;
CC P13928; O76024: WFS1; NbExp=3; IntAct=EBI-2556915, EBI-720609;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P13928-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13928-2; Sequence=VSP_056397, VSP_056398;
CC Name=3;
CC IsoId=P13928-3; Sequence=VSP_057805;
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; X16662; CAA34650.1; -; mRNA.
DR EMBL; M81844; AAB46383.1; -; mRNA.
DR EMBL; AK296573; BAG59193.1; -; mRNA.
DR EMBL; AK300158; BAG61941.1; -; mRNA.
DR EMBL; AL391137; CAI12203.1; -; Genomic_DNA.
DR EMBL; AL591684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004376; AAH04376.1; -; mRNA.
DR EMBL; BC073755; AAH73755.1; -; mRNA.
DR CCDS; CCDS73121.1; -. [P13928-3]
DR CCDS; CCDS73122.1; -. [P13928-1]
DR PIR; S06476; LUHU8.
DR RefSeq; NP_001035173.1; NM_001040084.2. [P13928-1]
DR RefSeq; NP_001092315.2; NM_001098845.2.
DR RefSeq; NP_001258631.1; NM_001271702.1.
DR RefSeq; NP_001258632.1; NM_001271703.1. [P13928-3]
DR PDB; 1W3W; X-ray; 1.99 A; A=1-327.
DR PDB; 1W45; X-ray; 2.51 A; A/B=1-327.
DR PDBsum; 1W3W; -.
DR PDBsum; 1W45; -.
DR AlphaFoldDB; P13928; -.
DR SMR; P13928; -.
DR BioGRID; 575558; 69.
DR BioGRID; 608549; 17.
DR IntAct; P13928; 31.
DR MINT; P13928; -.
DR iPTMnet; P13928; -.
DR PhosphoSitePlus; P13928; -.
DR SwissPalm; P13928; -.
DR BioMuta; ANXA8; -.
DR DMDM; 215274181; -.
DR EPD; P13928; -.
DR jPOST; P13928; -.
DR MassIVE; P13928; -.
DR MaxQB; P13928; -.
DR PaxDb; P13928; -.
DR PeptideAtlas; P13928; -.
DR PRIDE; P13928; -.
DR ProteomicsDB; 5097; -.
DR ProteomicsDB; 52998; -. [P13928-1]
DR Antibodypedia; 72811; 158 antibodies from 26 providers.
DR DNASU; 244; -.
DR Ensembl; ENST00000577813.1; ENSP00000463244.1; ENSG00000265190.7. [P13928-2]
DR Ensembl; ENST00000583911.5; ENSP00000463091.1; ENSG00000265190.7. [P13928-3]
DR Ensembl; ENST00000585281.6; ENSP00000462880.1; ENSG00000265190.7. [P13928-1]
DR GeneID; 653145; -.
DR GeneID; 728113; -.
DR KEGG; hsa:653145; -.
DR KEGG; hsa:728113; -.
DR MANE-Select; ENST00000585281.6; ENSP00000462880.1; NM_001040084.3; NP_001035173.1.
DR UCSC; uc001jev.5; human. [P13928-1]
DR CTD; 653145; -.
DR CTD; 728113; -.
DR DisGeNET; 653145; -.
DR DisGeNET; 728113; -.
DR GeneCards; ANXA8; -.
DR HGNC; HGNC:546; ANXA8.
DR HPA; ENSG00000265190; Tissue enhanced (esophagus, skin, vagina).
DR MIM; 602396; gene.
DR neXtProt; NX_P13928; -.
DR OpenTargets; ENSG00000265190; -.
DR PharmGKB; PA134881914; -.
DR PharmGKB; PA24836; -.
DR VEuPathDB; HostDB:ENSG00000265190; -.
DR GeneTree; ENSGT00940000161044; -.
DR HOGENOM; CLU_025300_2_3_1; -.
DR InParanoid; P13928; -.
DR OMA; RNESMNI; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P13928; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; P13928; -.
DR SignaLink; P13928; -.
DR BioGRID-ORCS; 653145; 6 hits in 970 CRISPR screens.
DR BioGRID-ORCS; 728113; 44 hits in 984 CRISPR screens.
DR ChiTaRS; ANXA8; human.
DR EvolutionaryTrace; P13928; -.
DR Pharos; P13928; Tbio.
DR PRO; PR:P13928; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P13928; protein.
DR Bgee; ENSG00000265190; Expressed in skin of abdomen and 89 other tissues.
DR ExpressionAtlas; P13928; baseline and differential.
DR Genevisible; P13928; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR009115; ANX8.
DR PANTHER; PTHR10502:SF133; PTHR10502:SF133; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01808; ANNEXINVIII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Annexin; Blood coagulation; Calcium;
KW Calcium/phospholipid-binding; Hemostasis; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..327
FT /note="Annexin A8"
FT /id="PRO_0000067503"
FT REPEAT 21..92
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 93..164
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 177..249
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 253..324
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT VAR_SEQ 8..69
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057805"
FT VAR_SEQ 138..141
FT /note="DYGS -> GQQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056397"
FT VAR_SEQ 142..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056398"
FT VARIANT 6
FT /note="S -> A (in dbSNP:rs3870786)"
FT /evidence="ECO:0000269|PubMed:2530088"
FT /id="VAR_000604"
FT VARIANT 177
FT /note="G -> A (in dbSNP:rs75345346)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2530088"
FT /id="VAR_030630"
FT CONFLICT 32
FT /note="K -> Q (in Ref. 3; BAG59193 and 4; CAI12203)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Q -> T (in Ref. 2; AAB46383)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="F -> L (in Ref. 2; AAB46383)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="R -> S (in Ref. 2; AAB46383)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..314
FT /note="GD -> RY (in Ref. 2; AAB46383)"
FT /evidence="ECO:0000305"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:1W3W"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1W3W"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1W3W"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1W45"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:1W3W"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 210..224
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:1W3W"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:1W3W"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:1W3W"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1W3W"
SQ SEQUENCE 327 AA; 36881 MW; 5DBBDBB6E723C298 CRC64;
MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA
KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL
ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV SSFVDPGLAL
QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL
EEAMLTVVKC TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG
KTLSSMIMED TSGDYKNALL SLVGSDP
